Faecal pellets in deep marine soft clay crusts: Implications for hot-oil pipeline design

In recent years, the presence of crusts within near surface sediments found in deep water locations off the west coast of Angola has been of interest to hot-oil pipeline designers. The origin for these crusts is considered to be of biological origin, based on the observation of thousands of faecal pellets in natural crust core samples. This paper presents the results of laboratory tests undertaken on natural and faecal pellet-only samples. These tests investigate the role faecal pellets play in modifying the gemechanical behaviour of clayey sediments. It is found that faecal pellets are able to significantly alter both the strength and the average grain-size of natural sediments, and therefore, influence the permeability and stiffness. Hot-oil pipelines self-embed into and subsequent shear on crusts containing faecal pellets. Being able to predict the time required for installed pipelines to consolidate the underlying sediment and thus, how soon after pipe-laying, the interface strength will develop is of great interest to pipeline designers. It is concluded from wet-sieving samples before and after oedometer tests, that the process of pipe laying is unlikely to destroy pellets. They will therefore, be a major constituent of the sediment subject to soil-pipeline shearing behaviour during axial pipe-walking and lateral buckling. Based on the presented results, a discussion highlighting the key implications for pipeline design is therefore provided. Copyright © 2011 by ASME.

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.

Ure2p is the protein determinant of the Saccharomyces cerevisiae prion state [URE3]. Constitutive overexpression of the HSP70 family member SSA1 cures cells of [URE3]. Here, we show that Ssa1p increases the lag time of Ure2p fibril formation in vitro in the presence or absence of nucleotide. The presence of the HSP40 co-chaperone Ydj1p has an additive effect on the inhibition of Ure2p fibril formation, whereas the Ydj1p H34Q mutant shows reduced inhibition alone and in combination with Ssa1p. In order to investigate the structural basis of these effects, we constructed and tested an Ssa1p mutant lacking the ATPase domain, as well as a series of C-terminal truncation mutants. The results indicate that Ssa1p can bind to Ure2p and delay fibril formation even in the absence of the ATPase domain, but interaction of Ure2p with the substrate-binding domain is strongly influenced by the C-terminal lid region. Dynamic light scattering, quartz crystal microbalance assays, pull-down assays and kinetic analysis indicate that Ssa1p interacts with both native Ure2p and fibril seeds, and reduces the rate of Ure2p fibril elongation in a concentration-dependent manner. These results provide new insights into the structural and mechanistic basis for inhibition of Ure2p fibril formation by Ssa1p and Ydj1p.